2pi0: Difference between revisions

Line 4:

==Overview==

Interferon regulatory factor 3 (IRF-3) is a key transcription factor in, the assembly of the mammalian interferon-beta (IFN-beta) enhanceosome. We, present here the structure of IRF-3 DNA binding domain in complex with the, complete PRDIII-I regulatory element of the human IFN-beta enhancer. We, show that four IRF-3 molecules bind in tandem to, variably spaced, consensus and nonconsensus IRF sites on the composite element. The ability, of IRF-3 to bind these variable sites derives in part from two, nonconserved arginines (Arg78 and Arg86) that partake in alternate, protein-DNA contacts. We also show that the protein-DNA contacts are, highly overlapped and that all four IRF sites are required for gene, activation in vivo. In addition, we show that changing the nonconsensus, IRF sites to consensus sites creates a more efficient enhancer in vivo., Together, the structure and accompanying biological data provide insights, into the assembly of the IFN-beta enhanceosome in mammals.

Interferon regulatory factor 3 (IRF-3) is a key transcription factor in the assembly of the mammalian interferon-beta (IFN-beta) enhanceosome. We present here the structure of IRF-3 DNA binding domain in complex with the complete PRDIII-I regulatory element of the human IFN-beta enhancer. We show that four IRF-3 molecules bind in tandem to, variably spaced, consensus and nonconsensus IRF sites on the composite element. The ability of IRF-3 to bind these variable sites derives in part from two nonconserved arginines (Arg78 and Arg86) that partake in alternate protein-DNA contacts. We also show that the protein-DNA contacts are highly overlapped and that all four IRF sites are required for gene activation in vivo. In addition, we show that changing the nonconsensus IRF sites to consensus sites creates a more efficient enhancer in vivo. Together, the structure and accompanying biological data provide insights into the assembly of the IFN-beta enhanceosome in mammals.

==About this Structure==

Line 13:

[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Aggarwal, A.K.]]

[[Category: Aggarwal, A K.]]

[[Category: Escalante, C.R.]]

[[Category: Escalante, C R.]]

[[Category: Garcia-Sastre, A.]]

[[Category: Leyi, S.]]

Line 23:

[[Category: transcription activator/dna complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 12~~:36:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:41 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Interferon regulatory factor 3 (IRF-3) is a key transcription factor in, the assembly of the mammalian interferon-beta (IFN-beta) enhanceosome. We, present here the structure of IRF-3 DNA binding domain in complex with the, complete PRDIII-I regulatory element of the human IFN-beta enhancer. We, show that four IRF-3 molecules bind in tandem to, variably spaced, consensus and nonconsensus IRF sites on the composite element. The ability, of IRF-3 to bind these variable sites derives in part from two, nonconserved arginines (Arg78 and Arg86) that partake in alternate, protein-DNA contacts. We also show that the protein-DNA contacts are, highly overlapped and that all four IRF sites are required for gene, activation in vivo. In addition, we show that changing the nonconsensus, IRF sites to consensus sites creates a more efficient enhancer in vivo., Together, the structure and accompanying biological data provide insights, into the assembly of the IFN-beta enhanceosome in mammals.
+Interferon regulatory factor 3 (IRF-3) is a key transcription factor in the assembly of the mammalian interferon-beta (IFN-beta) enhanceosome. We present here the structure of IRF-3 DNA binding domain in complex with the complete PRDIII-I regulatory element of the human IFN-beta enhancer. We show that four IRF-3 molecules bind in tandem to, variably spaced, consensus and nonconsensus IRF sites on the composite element. The ability of IRF-3 to bind these variable sites derives in part from two nonconserved arginines (Arg78 and Arg86) that partake in alternate protein-DNA contacts. We also show that the protein-DNA contacts are highly overlapped and that all four IRF sites are required for gene activation in vivo. In addition, we show that changing the nonconsensus IRF sites to consensus sites creates a more efficient enhancer in vivo. Together, the structure and accompanying biological data provide insights into the assembly of the IFN-beta enhanceosome in mammals.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Aggarwal, A.K.]]
+[[Category: Aggarwal, A K.]]
-[[Category: Escalante, C.R.]]
+[[Category: Escalante, C R.]]
 [[Category: Garcia-Sastre, A.]]
 [[Category: Leyi, S.]]
@@ Line 23: / Line 23: @@
 [[Category: transcription activator/dna complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:36:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:41 2008''